ID   ACDH_POLNA              Reviewed;         304 AA.
AC   A1VUV2;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Acetaldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01657};
DE            EC=1.2.1.10 {ECO:0000255|HAMAP-Rule:MF_01657};
DE   AltName: Full=Acetaldehyde dehydrogenase [acetylating] {ECO:0000255|HAMAP-Rule:MF_01657};
GN   OrderedLocusNames=Pnap_4143;
OS   Polaromonas naphthalenivorans (strain CJ2).
OG   Plasmid pPNAP01.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2;
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetaldehyde + CoA + NAD(+) = acetyl-CoA + H(+) + NADH;
CC         Xref=Rhea:RHEA:23288, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:57945; EC=1.2.1.10; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01657};
CC   -!- SIMILARITY: Belongs to the acetaldehyde dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01657}.
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DR   EMBL; CP000530; ABM39430.1; -; Genomic_DNA.
DR   RefSeq; WP_011797809.1; NC_008757.1.
DR   AlphaFoldDB; A1VUV2; -.
DR   SMR; A1VUV2; -.
DR   EnsemblBacteria; ABM39430; ABM39430; Pnap_4143.
DR   KEGG; pna:Pnap_4143; -.
DR   HOGENOM; CLU_062208_0_0_4; -.
DR   OMA; TSAYVHK; -.
DR   OrthoDB; 1432332at2; -.
DR   Proteomes; UP000000644; Plasmid pPNAP01.
DR   GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019439; P:aromatic compound catabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_01657; Ac_ald_DH_ac; 1.
DR   InterPro; IPR003361; Acetaldehyde_dehydrogenase.
DR   InterPro; IPR015426; Acetylaldehyde_DH_C.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR000534; Semialdehyde_DH_NAD-bd.
DR   Pfam; PF09290; AcetDehyd-dimer; 1.
DR   Pfam; PF01118; Semialdhyde_dh; 1.
DR   PIRSF; PIRSF015689; Actaldh_dh_actl; 1.
DR   SMART; SM00859; Semialdhyde_dh; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR03215; ac_ald_DH_ac; 1.
PE   3: Inferred from homology;
KW   Aromatic hydrocarbons catabolism; NAD; Oxidoreductase; Plasmid;
KW   Reference proteome.
FT   CHAIN           1..304
FT                   /note="Acetaldehyde dehydrogenase"
FT                   /id="PRO_0000387703"
FT   ACT_SITE        131
FT                   /note="Acyl-thioester intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         162..170
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
FT   BINDING         273
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01657"
SQ   SEQUENCE   304 AA;  32279 MW;  96D94FB2297DECBB CRC64;
     MTKKIKCALI GPGNIGTDLL AKLQRSAVLE PVWMVGIDPE SDGLKRAREM GIKTTADGVD
     GLIPHMQADG VQIVFDATSA YVHAENSRKV NAQGALMIDL TPAAIGPFCV PPVNLIEHVG
     KGEMNVNMVT CGGQATIPMV AAVSRVQPVA YGEIIATVSS KSAGPGTRKN IDEFTRTTAS
     AVEKVGGAKK GKAIIILNPA EPPLIMRDTV HCLLESEPDQ AKITESIHAM IQEVQKYVPG
     YKLVNGPVFD GKRVSVFLEV EGLGDYLPKY AGNLDIMTAA AARTAEMFAE EILAGRLTLK
     PVHA